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    TREX2 three prime repair exonuclease 2 [ Homo sapiens (human) ]

    Gene ID: 11219, updated on 10-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The Human TREX-2 Complex Interacts with Subunits of the ORC Complex.

    The Human TREX-2 Complex Interacts with Subunits of the ORC Complex.
    Kurshakova MM, Georgieva SG, Kopytova DV., Free PMC Article

    02/5/2024
    TREX2 Exonuclease Causes Spontaneous Mutations and Stress-Induced Replication Fork Defects in Cells Expressing RAD51(K133A).

    TREX2 Exonuclease Causes Spontaneous Mutations and Stress-Induced Replication Fork Defects in Cells Expressing RAD51(K133A).
    Ko JH, Son MY, Zhou Q, Molnarova L, Song L, Mlcouskova J, Jekabsons A, Montagna C, Krejci L, Hasty P., Free PMC Article

    12/25/2021
    Nucleoporin TPR is an integral component of the TREX-2 mRNA export pathway.

    Nucleoporin TPR is an integral component of the TREX-2 mRNA export pathway.
    Aksenova V, Smith A, Lee H, Bhat P, Esnault C, Chen S, Iben J, Kaufhold R, Yau KC, Echeverria C, Fontoura B, Arnaoutov A, Dasso M., Free PMC Article

    10/3/2020
    Significant methylation loss at an intragenic site of TREX2 was a frequent trait in a cohort of patients with laryngeal cancer. Methylation loss correlated with increased expression of TREX2 in laryngeal tumors and improved overall survival. These data highlight a regulatory role of TREX2 DNA methylation for gene expression which might affect incidence and survival of laryngeal cancer.

    DNA methylation at an enhancer of the three prime repair exonuclease 2 gene (TREX2) is linked to gene expression and survival in laryngeal cancer.
    Weigel C, Chaisaingmongkol J, Assenov Y, Kuhmann C, Winkler V, Santi I, Bogatyrova O, Kaucher S, Bermejo JL, Leung SY, Chan TL, Lasitschka F, Bohrer MH, Marx A, Haußen RH, Herold-Mende C, Dyckhoff G, Boukamp P, Delank KW, Hörmann K, Lippert BM, Baier G, Dietz A, Oakes CC, Plass C, Becher H, Schmezer P, Ramroth H, Popanda O., Free PMC Article

    03/21/2020
    the scaffold subunit of TREX-2, GANP, positively regulates DNA repair through homologous recombination (HR). In contrast, DUBm adaptor subunits ENY2 and ATXNL3 are required to limit unscheduled HR.

    Transcription and mRNA export machineries SAGA and TREX-2 maintain monoubiquitinated H2B balance required for DNA repair.
    Evangelista FM, Maglott-Roth A, Stierle M, Brino L, Soutoglou E, Tora L., Free PMC Article

    09/28/2019
    Altogether, data provide new insights in the molecular mechanisms of TREX2 activity and establish cell autonomous and non-cell autonomous functions of TREX2 in the UVB-induced skin response.

    Multifaceted role of TREX2 in the skin defense against UV-induced skin carcinogenesis.
    Manils J, Gómez D, Salla-Martret M, Fischer H, Fye JM, Marzo E, Marruecos L, Serrano I, Salgado R, Rodrigo JP, Garcia-Pedrero JM, Serafin AM, Cañas X, Benito C, Toll A, Forcales SV, Perrino FW, Eckhart L, Soler C., Free PMC Article

    10/1/2016
    human TREX-2 complex prevents genome instability, as determined by the accumulation of gamma-H2AX and 53BP1 foci and single-cell electrophoresis in cells depleted of the TREX-2 subunits PCID2, GANP and DSS1

    BRCA2 prevents R-loop accumulation and associates with TREX-2 mRNA export factor PCID2.
    Bhatia V, Barroso SI, García-Rubio ML, Tumini E, Herrera-Moyano E, Aguilera A.

    08/23/2014
    TREX-2 is an NPC-associated complex in mammalian cells.

    The human TREX-2 complex is stably associated with the nuclear pore basket.
    Umlauf D, Bonnet J, Waharte F, Fournier M, Stierle M, Fischer B, Brino L, Devys D, Tora L.

    03/1/2014
    Trex2 does not enable DSB repair and prompt a new model that posits Trex2 suppresses the formation of broken chromosomes.

    Trex2 enables spontaneous sister chromatid exchanges without facilitating DNA double-strand break repair.
    Dumitrache LC, Hu L, Son MY, Li H, Wesevich A, Scully R, Stark J, Hasty P., Free PMC Article

    12/24/2011
    a model for DNA binding and 3' hydrolysis for the TREX2 dimer.

    DNA binding induces active site conformational change in the human TREX2 3'-exonuclease.
    de Silva U, Perrino FW, Hollis T., Free PMC Article

    01/21/2010
    Trex2 deletion caused high levels of Robertsonian translocations (RbTs) showing Trex2 is important for chromosomal maintenance.

    TREX2 exonuclease defective cells exhibit double-strand breaks and chromosomal fragments but not Robertsonian translocations.
    Dumitrache LC, Hu L, Hasty P., Free PMC Article

    01/21/2010
    analysis of cooperative DNA binding and communication across the dimer interface in the TREX2 3' --> 5'-exonuclease

    Cooperative DNA binding and communication across the dimer interface in the TREX2 3' --> 5'-exonuclease.
    Perrino FW, de Silva U, Harvey S, Pryor EE Jr, Cole DW, Hollis T., Free PMC Article

    01/21/2010
    Observational study of gene-disease association. (HuGE Navigator)

    TREX1 polymorphisms associated with autoantibodies in patients with systemic lupus erythematosus.
    Hur JW, Sung YK, Shin HD, Park BL, Cheong HS, Bae SC.

    03/13/2008
    Polymorphisms exist in prostatic cancer patients.

    Sequence variants in the 3'-->5' deoxyribonuclease TREX2: identification in a genetic screen and effects on catalysis by the recombinant proteins.
    Perrino FW, Krol A, Harvey S, Zheng SL, Horita DA, Hollis T, Meyers DA, Isaacs WB, Xu J.

    01/21/2010
    analysis of human TREX2 3' -> 5'-exonuclease structure and description of the mechanism for efficient nonprocessive DNA catalysis

    The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis.
    Perrino FW, Harvey S, McMillin S, Hollis T.

    01/21/2010
    Results suggest that TREX2 plays an important function during DNA metabolism and cellular proliferation.

    Biochemical and cellular characteristics of the 3' -> 5' exonuclease TREX2.
    Chen MJ, Ma SM, Dumitrache LC, Hasty P., Free PMC Article

    01/21/2010
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